Accounting for Conformational Variability in NMR Structure of Cyclopeptides: Ensemble Averaging of Interproton Distance and Coupling Constant Restraints-Reference-Cited by-同舟云学术

Accounting for Conformational Variability in NMR Structure of Cyclopeptides: Ensemble Averaging of Interproton Distance and Coupling Constant Restraints

Published:1997-06-01 Issue:22 Volume:119 Page:5239-5248
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Cuniasse Philippe¹,Raynal Isabelle¹,Yiotakis Athanosios¹,Dive Vincent¹

Affiliation:

1. Contribution from the Département d'Ingénierie et d'Etudes des Protéines D.S.V., CEA/Saclay, 91191 Gif sur Yvette Cedex, France, and Department of Organic Chemistry, Laboratory of Organic Chemistry, University of Athens, Panepistimiopolis Zografou, Greece

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9636810

Reference75 articles.

1. CONSTRAINED PEPTIDES: MODELS OF BIOACTIVE PEPTIDES AND PROTEIN SUBSTRUCTURES

2. Vicinal Proton Coupling in Nuclear Magnetic Resonance

3. Calculation of protein conformations by proton-proton distance constraints

4. Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms Circumventing problems associated with folding

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